ID   KHK_PONAB               Reviewed;         297 AA.
AC   Q5RD71;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Ketohexokinase;
DE            EC=2.7.1.3;
DE   AltName: Full=Hepatic fructokinase;
GN   Name=KHK;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of the ketose sugar fructose to
CC       fructose-1-phosphate. {ECO:0000250|UniProtKB:P50053}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose = ADP + beta-D-fructose 1-phosphate +
CC         H(+); Xref=Rhea:RHEA:18145, ChEBI:CHEBI:15378, ChEBI:CHEBI:28645,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:138881, ChEBI:CHEBI:456216;
CC         EC=2.7.1.3;
CC   -!- ACTIVITY REGULATION: Requires potassium. Inhibition by ADP (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Carbohydrate metabolism; fructose metabolism.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P50053}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000305}.
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DR   EMBL; CR858045; CAH90286.1; -; Transcribed_RNA.
DR   AlphaFoldDB; Q5RD71; -.
DR   SMR; Q5RD71; -.
DR   STRING; 9601.ENSPPYP00000014032; -.
DR   eggNOG; KOG2947; Eukaryota.
DR   InParanoid; Q5RD71; -.
DR   UniPathway; UPA00202; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004454; F:ketohexokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006000; P:fructose metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01939; Ketohexokinase; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR034093; KHK.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR029056; Ribokinase-like.
DR   Pfam; PF00294; PfkB; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..297
FT                   /note="Ketohexokinase"
FT                   /id="PRO_0000080090"
FT   BINDING         15
FT                   /ligand="beta-D-fructose"
FT                   /ligand_id="ChEBI:CHEBI:28645"
FT                   /evidence="ECO:0000250|UniProtKB:P50053"
FT   BINDING         41
FT                   /ligand="beta-D-fructose"
FT                   /ligand_id="ChEBI:CHEBI:28645"
FT                   /evidence="ECO:0000250|UniProtKB:P50053"
FT   BINDING         42
FT                   /ligand="beta-D-fructose"
FT                   /ligand_id="ChEBI:CHEBI:28645"
FT                   /evidence="ECO:0000250|UniProtKB:P50053"
FT   BINDING         45
FT                   /ligand="beta-D-fructose"
FT                   /ligand_id="ChEBI:CHEBI:28645"
FT                   /evidence="ECO:0000250|UniProtKB:P50053"
FT   BINDING         107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P50053"
FT   BINDING         225..228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P50053"
FT   BINDING         254..257
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P50053"
FT   BINDING         257
FT                   /ligand="beta-D-fructose"
FT                   /ligand_id="ChEBI:CHEBI:28645"
FT                   /evidence="ECO:0000250|UniProtKB:P50053"
SQ   SEQUENCE   297 AA;  32476 MW;  049C7C1FA74DEF16 CRC64;
     MEEKQILCVG LVVLDVISLV DKYPKEDSEI RCLSQRWQRG GNASNSCTVL SLLGAPCAFM
     GSMAPGHVAF LVADFRRRGV DVSQVAWQSK GDTPSSCCII NNSNGNRTIV LHDTSLPDVS
     ATDFEKVDLT QFKWIHIEGR NASEQVKMLQ RIDTHNTRQP PEQKIRVSVE VEKPQEELFQ
     LFGYGDVVFV SKDVAKHLGF QSAEAALRGL YGRVRKGAVL VCAWAEEGAD ALGPDDKLFH
     SDAFPPPRVV DTLGAGDTFN ASVIFSLSQG RSMQEALRFG CQVAGKKCGL QGFDGIV